EP0524220A1 - A pulping process using cellulase. - Google Patents

A pulping process using cellulase.

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Publication number
EP0524220A1
EP0524220A1 EP91907253A EP91907253A EP0524220A1 EP 0524220 A1 EP0524220 A1 EP 0524220A1 EP 91907253 A EP91907253 A EP 91907253A EP 91907253 A EP91907253 A EP 91907253A EP 0524220 A1 EP0524220 A1 EP 0524220A1
Authority
EP
European Patent Office
Prior art keywords
cellulase
pulp
pulping
consistency
enzyme
Prior art date
Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
Granted
Application number
EP91907253A
Other languages
German (de)
French (fr)
Other versions
EP0524220B1 (en
Inventor
Jean-Luc Alain Guy Baret
Marc Leclerc
Current Assignee (The listed assignees may be inaccurate. Google has not performed a legal analysis and makes no representation or warranty as to the accuracy of the list.)
Novozymes AS
Original Assignee
Novo Nordisk AS
Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.)
Filing date
Publication date
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Application filed by Novo Nordisk AS filed Critical Novo Nordisk AS
Publication of EP0524220A1 publication Critical patent/EP0524220A1/en
Application granted granted Critical
Publication of EP0524220B1 publication Critical patent/EP0524220B1/en
Anticipated expiration legal-status Critical
Revoked legal-status Critical Current

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Classifications

    • CCHEMISTRY; METALLURGY
    • C12BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12NMICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N9/00Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/14Hydrolases (3)
    • C12N9/24Hydrolases (3) acting on glycosyl compounds (3.2)
    • C12N9/2402Hydrolases (3) acting on glycosyl compounds (3.2) hydrolysing O- and S- glycosyl compounds (3.2.1)
    • C12N9/2405Glucanases
    • C12N9/2434Glucanases acting on beta-1,4-glucosidic bonds
    • C12N9/2437Cellulases (3.2.1.4; 3.2.1.74; 3.2.1.91; 3.2.1.150)
    • CCHEMISTRY; METALLURGY
    • C12BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12YENZYMES
    • C12Y302/00Hydrolases acting on glycosyl compounds, i.e. glycosylases (3.2)
    • C12Y302/01Glycosidases, i.e. enzymes hydrolysing O- and S-glycosyl compounds (3.2.1)
    • C12Y302/01004Cellulase (3.2.1.4), i.e. endo-1,4-beta-glucanase
    • DTEXTILES; PAPER
    • D21PAPER-MAKING; PRODUCTION OF CELLULOSE
    • D21CPRODUCTION OF CELLULOSE BY REMOVING NON-CELLULOSE SUBSTANCES FROM CELLULOSE-CONTAINING MATERIALS; REGENERATION OF PULPING LIQUORS; APPARATUS THEREFOR
    • D21C5/00Other processes for obtaining cellulose, e.g. cooking cotton linters ; Processes characterised by the choice of cellulose-containing starting materials
    • D21C5/005Treatment of cellulose-containing material with microorganisms or enzymes
    • DTEXTILES; PAPER
    • D21PAPER-MAKING; PRODUCTION OF CELLULOSE
    • D21HPULP COMPOSITIONS; PREPARATION THEREOF NOT COVERED BY SUBCLASSES D21C OR D21D; IMPREGNATING OR COATING OF PAPER; TREATMENT OF FINISHED PAPER NOT COVERED BY CLASS B31 OR SUBCLASS D21G; PAPER NOT OTHERWISE PROVIDED FOR
    • D21H17/00Non-fibrous material added to the pulp, characterised by its constitution; Paper-impregnating material characterised by its constitution
    • D21H17/005Microorganisms or enzymes
    • DTEXTILES; PAPER
    • D21PAPER-MAKING; PRODUCTION OF CELLULOSE
    • D21HPULP COMPOSITIONS; PREPARATION THEREOF NOT COVERED BY SUBCLASSES D21C OR D21D; IMPREGNATING OR COATING OF PAPER; TREATMENT OF FINISHED PAPER NOT COVERED BY CLASS B31 OR SUBCLASS D21G; PAPER NOT OTHERWISE PROVIDED FOR
    • D21H21/00Non-fibrous material added to the pulp, characterised by its function, form or properties; Paper-impregnating or coating material, characterised by its function, form or properties
    • D21H21/06Paper forming aids
    • D21H21/10Retention agents or drainage improvers

Definitions

  • This invention relates to a pulping process wherein cellulase is used to improve the drainage properties of the pulp.
  • the drainage properties of the pulp may in some cases be unsatisfactory, whereby the capacity of the paper line may be reduced.
  • the drainage properties of the pulp are commonly estimated by the Schopper-Riegler test (a high SR value indicating poor drainage) or by Canadian Standard Freeness (a low CSF value indicating poor drainage). Unsatisfactory drainage may particularly occur in case of repulping material that has already been through a pulping and drying process, e.g. dried virgin pulp, recycled fibre or waste paper.
  • EP 262,040 Cellulose du Pin
  • EP 351 ,655 Cellultor
  • J-C Pommier et al., TAPPI Journal, June 1989, pp. 187-191 indicate that 3% consistency is optimum for drainage improvement by cellulase treatment (as indicated by CSF), and that the effect decreases significantly from 3 to 5%.
  • JP-A 59-9299 and JP-A 63-59494 describe use of cellulase during pulping at 3-6% consistency at high pH (above 9) to improve ink removal from waste paper. High-consistency pulping at consistency above 8%, typically 10-20%, is commonly used, but use of cellulase in this type of process has not been described.
  • drainability can be further improved when the cellulase is used during pulping at high consistency (above 8%).
  • the invention provides a pulping process wherein cellulase is used to improve the drainage properties of the pulp, characterized by a consistency above 8%.
  • the process of the invention can be applied to any pulp where it is desired to improve drainability. This is particularly of interest for pulps with SR value above 25 or CSF value below 50, and particularly for repulping of previously pulped and dried material such as dried virgin pulp, recycled fibres and waste paper.
  • cellulase Many types are known and can be used in the process of the invention. Microbial cellulase are preferred for reasons of economy.
  • the cellulase should be active and stable at the conditions, especially the pH, of the process.
  • suitable cellulases are those derived from Asper ⁇ illus (particularly A. niqer). Trichoderma (particularly T. viride. T. reesei and T. koningii), Humicola (particularly H. insolens. see US 4,435,307) and alkalophilic Bacillus (US 3,844,890).
  • Examples of commercial cellulase preparations are Novozym ⁇ 342 (H. insolens) and Celluclast 1.5L (T. reesei). both available from Novo-Nordisk A/S.
  • a suitable cellulase dosage will usually correspond to a cellulase activity at pH 6 of 100 - 10,000 EGU/kg of dry pulp. Where the pulping process is at alkaline pH (above 7), the cellulase dosage should correspond to a cellulase activity at pH 9 of 100 - 10,000 CEVU/kg of dry pulp.
  • the duration of the pulping will generally be 5 - 30 minutes, and this may optionally be followed by maceration (i.e. incubation with or without stirring) to let the enzyme action continue.
  • the temperature throughout this treatment will generally be 15-60"C, typically 30-50 ⁇ C.
  • the total duration of the cellulase action i.e. pulping + maceration, if any) will generally be 30-180 minutes.
  • Pulp prepared according to the invention can be used for conventional paper making.
  • a substrate solution is prepared, containing 34.0 g/l CMC (Hercules 7 LFD) in 0.1 M phosphate buffer at pH 6.0.
  • the enzyme sample to be analyzed is dissolved in the same buffer.
  • 10 ml substrate solution and 0.5 ml enzyme solution are mixed and transferred to a vibration viscosimeter (e.g. MIVI 3000 from Sofraser, France), thermostated at 40° C.
  • MIVI 3000 from Sofraser, France
  • One Endo-Glucanase Unit (EGU) is defined as the amount of enzyme that reduces the viscosity to one half under these conditions.
  • a substrate solution is prepared, containing 33.3 g/l CMC (Hercules 7 LFD) in 0.1 M Tris buffer at pH 9.0.
  • the enzyme sample to be analyzed is dissolved in the same buffer.
  • 10 ml substrate solution and 0.5 ml enzyme solution are mixed and transferred to a viscosimeter (e.g. Haake VT 181, NV sensor, 181 rpm) thermostated at 40° C.
  • a viscosimeter e.g. Haake VT 181, NV sensor, 181 rpm
  • One Cellulase Viscosity Unit is defined as the amount of enzyme that reduces the viscosity to one half under these conditions.
  • the first type of pulp is a raw mechanical pulp from decidous tree, and the second type is a bleached kraft pulp.
  • the dry pulps are disintegrated in a 20 litres high consistency lab pulper with warm water.
  • the mechanical pulp and the bleached kraft pulp are disintegrated at 8 and 10% consistency, respectively.
  • Their pH is then adjusted to 5.0 with diluted sulfuric acid.
  • the enzyme preparation Celluclast® 1.5L (activity 840 EGU/g) is added to the pulps at the dose of 5 kg/t dry pulp.
  • For each pulp a control experiment without enzyme is also made. In all experiments the temperature is maintained at 45°C +/- 1 ⁇ C and the pH at 5.0 +/- 0.1.
  • the SR is measured after 90 minutes pulping.
  • the following tables show the resulting SR numbers for both pulps:
  • the cardboards are disintegrated at 8% consistency in a 20 litres lab pulper. Their pH is then adjusted to values ranging from 7.6 to 10.1 with diluted sodium hydroxide.
  • the enzyme preparation Novozym® 342 (1030 CEVU/g) is added to the pulps at the dose of 5 kg/t dry pulp. For each pulp a control experiment without enzyme is also made. In all experiments the temperature is maintained at 45" C +/- 1 "C.
  • the Schopper-Riegler number (SR) is measured after 90 minutes pulping. The following tables show the resulting SR numbers for the different pH values:
  • pulped for 20 minutes at high consistency in a 20 litres lab pulper then macerated without stirring.
  • the enzyme Novozym® 342 is added at the beginning of the pulping.
  • the pulps are raw mechancial pulp, bleached mechanical pulp, and bleached kraft pulp.

Abstract

In the preparation of pulp for paper making, the drainage properties can be improved by treating the pulp with cellulase at high pulp consistency (above 8 %).

Description

A PROCESS USING CELLULASE FOR IMPROVING DRAINAGE PROPERTIES OF PULP
TECHNICAL FIELD
This invention relates to a pulping process wherein cellulase is used to improve the drainage properties of the pulp.
BACKGROUND ART
In the preparation of pulp for paper making, the drainage properties of the pulp may in some cases be unsatisfactory, whereby the capacity of the paper line may be reduced. The drainage properties of the pulp are commonly estimated by the Schopper-Riegler test (a high SR value indicating poor drainage) or by Canadian Standard Freeness (a low CSF value indicating poor drainage). Unsatisfactory drainage may particularly occur in case of repulping material that has already been through a pulping and drying process, e.g. dried virgin pulp, recycled fibre or waste paper.
EP 262,040 (Cellulose du Pin) and EP 351 ,655 (Cultor) describe improved drainability by use of cellulase and hemicellulase during pulping. The consistency (i.e. % dry matter concentration) was 2 - 5%.
J-C Pommier et al., TAPPI Journal, June 1989, pp. 187-191 indicate that 3% consistency is optimum for drainage improvement by cellulase treatment (as indicated by CSF), and that the effect decreases significantly from 3 to 5%. JP-A 59-9299 and JP-A 63-59494 describe use of cellulase during pulping at 3-6% consistency at high pH (above 9) to improve ink removal from waste paper. High-consistency pulping at consistency above 8%, typically 10-20%, is commonly used, but use of cellulase in this type of process has not been described.
It is the object of the invention to provide an improved process.
STATEMENT OF THE INVENTION
We have surprisingly found that drainability can be further improved when the cellulase is used during pulping at high consistency (above 8%).
Accordingly, the invention provides a pulping process wherein cellulase is used to improve the drainage properties of the pulp, characterized by a consistency above 8%.
DETAILED DESCRIPTION
Raw material
The process of the invention can be applied to any pulp where it is desired to improve drainability. This is particularly of interest for pulps with SR value above 25 or CSF value below 50, and particularly for repulping of previously pulped and dried material such as dried virgin pulp, recycled fibres and waste paper.
Cellulase
Many types of cellulase are known and can be used in the process of the invention. Microbial cellulase are preferred for reasons of economy. The cellulase should be active and stable at the conditions, especially the pH, of the process. Some examples of suitable cellulases are those derived from Asperαillus (particularly A. niqer). Trichoderma (particularly T. viride. T. reesei and T. koningii), Humicola (particularly H. insolens. see US 4,435,307) and alkalophilic Bacillus (US 3,844,890). Examples of commercial cellulase preparations are Novozymβ 342 (H. insolens) and Celluclast 1.5L (T. reesei). both available from Novo-Nordisk A/S.
A suitable cellulase dosage will usually correspond to a cellulase activity at pH 6 of 100 - 10,000 EGU/kg of dry pulp. Where the pulping process is at alkaline pH (above 7), the cellulase dosage should correspond to a cellulase activity at pH 9 of 100 - 10,000 CEVU/kg of dry pulp.
Pulping process
The process is carried out at a consistency above 8%, typically 10- 20%. The cellulase can be added in an existing high-consistency pulping process using any type of known high-consistency pulper. Depending e.g. on the use of recycled water, the process may be acidic (e.g. pH 4 - 6) where Asperqillus or Trichoderma cellulase is preferred. Or, the process pH may be near-neutral (e.g. pH 6 - 8) where Humicola or Bacillus cellulase is preferred.
When the process of the invention is to be applied to pulping of waste paper, deinking can be achieved by carrying out the pulping at high pH (above 9) in the presence of deinking chemicals (such as sodium hydroxide, sodium silicate, hydrogen peroxide and surfactant), followed by ink separation (e.g. by flotation and/or rinsing). This embodiment of the invention is particularly advantageous since the cellulase will also serve to improve the deinking, while at the same time improving drainage. At the high pH used for deinking, it is preferred to use cellulase from Humicola or alkaline Bacillus.
The duration of the pulping will generally be 5 - 30 minutes, and this may optionally be followed by maceration (i.e. incubation with or without stirring) to let the enzyme action continue. The temperature throughout this treatment will generally be 15-60"C, typically 30-50 βC. The total duration of the cellulase action (i.e. pulping + maceration, if any) will generally be 30-180 minutes.
Pulp prepared according to the invention can be used for conventional paper making.
EXAMPLES
Determination of cellulase activity at pH 6 (EGU)
A substrate solution is prepared, containing 34.0 g/l CMC (Hercules 7 LFD) in 0.1 M phosphate buffer at pH 6.0. The enzyme sample to be analyzed is dissolved in the same buffer. 10 ml substrate solution and 0.5 ml enzyme solution are mixed and transferred to a vibration viscosimeter (e.g. MIVI 3000 from Sofraser, France), thermostated at 40° C. One Endo-Glucanase Unit (EGU) is defined as the amount of enzyme that reduces the viscosity to one half under these conditions.
Determination of cellulase activity at pH 9 (CEVU)
A substrate solution is prepared, containing 33.3 g/l CMC (Hercules 7 LFD) in 0.1 M Tris buffer at pH 9.0. The enzyme sample to be analyzed is dissolved in the same buffer. 10 ml substrate solution and 0.5 ml enzyme solution are mixed and transferred to a viscosimeter (e.g. Haake VT 181, NV sensor, 181 rpm) thermostated at 40° C. One Cellulase Viscosity Unit (CEVU) is defined as the amount of enzyme that reduces the viscosity to one half under these conditions.
Determination of pulp drainage (Schopper-Riegler)
The Schopper-Riegler number (SR) is determined according to ISO standard 5267 (part 1), on a homogenous pulp at a consistency of 2 g/l. A known volume of pulp is allowed to drain through a metal sieve into a funnel. This funnel has an axial hole and a side hole. The volume of filtrate that has passed through the side hole is measured in a special vessel graduated in Schopper-Riegler units.
EXAMPLE 1
In this example two types of pulps are pulped at high consistency together with an enzyme treatment by the cellulase preparation Celluclast® 1.5L. The first type of pulp is a raw mechanical pulp from decidous tree, and the second type is a bleached kraft pulp.
The dry pulps are disintegrated in a 20 litres high consistency lab pulper with warm water. The mechanical pulp and the bleached kraft pulp are disintegrated at 8 and 10% consistency, respectively. Their pH is then adjusted to 5.0 with diluted sulfuric acid. The enzyme preparation Celluclast® 1.5L (activity 840 EGU/g) is added to the pulps at the dose of 5 kg/t dry pulp. For each pulp a control experiment without enzyme is also made. In all experiments the temperature is maintained at 45°C +/- 1 βC and the pH at 5.0 +/- 0.1. The SR is measured after 90 minutes pulping. The following tables show the resulting SR numbers for both pulps:
The action of the enzyme resulted in a SR decrease of 7 points for the mechanical pulp and 8 points for the bleached kraft pulp.
EXAMPLE 2
In this example a mix of old cardboard containers is pulped at high consistency together with an enzyme treatment by the cellulase preparation Novozym® 342, at several pH values.
The cardboards are disintegrated at 8% consistency in a 20 litres lab pulper. Their pH is then adjusted to values ranging from 7.6 to 10.1 with diluted sodium hydroxide. The enzyme preparation Novozym® 342 (1030 CEVU/g) is added to the pulps at the dose of 5 kg/t dry pulp. For each pulp a control experiment without enzyme is also made. In all experiments the temperature is maintained at 45" C +/- 1 "C. The Schopper-Riegler number (SR) is measured after 90 minutes pulping. The following tables show the resulting SR numbers for the different pH values:
pH 7.6 Novozym® 342 29
Control 38
Difference 9
pH 9.1 Novozym® 342 32
Control 39 Difference 7
pH 9.6 Novozym® 342 33 Control 38
Difference 5
pH 10.1 Novozym® 342 37 Control 38
Difference 1 The action of Novozym® 342 at various alkaline pH's results in a drainability improvement of 1 to 9 SR points. That can be compared to experiments on the same cardboards where the pulp is incubated with or without the enzyme at 3% consistency instead of 8%. In this case the SR gain provided by the enzyme is only 6 points at pH 7.6 and 2 points at pH 9.1. It is nil at higher pH values. This illustrates the positive effect of high consistency on the SR- reducing action of Novozym® 342 at high pH.
EXAMPLE 3
In this example three types of pulp are pulped for 20 minutes at high consistency in a 20 litres lab pulper, then macerated without stirring. The enzyme Novozym® 342 is added at the beginning of the pulping. The pulps are raw mechancial pulp, bleached mechanical pulp, and bleached kraft pulp.
Two sets of experiments are made: one at the natural pH of the pulp (7.5), and one at pH 9.5. The pH of the pulp is adjusted with diluted sodium hydroxide at the beginning of the pulping, prior to eventual enzyme addition. The enzyme preparation Novozym® 342 (1030 CEVU/g) is added to the pulps at the dose of 2.5 kg/t dry pulp. For each pulp a control experiment without enzyme is also made. In all experiments the temperature is maintained at 45 "C +/- 1 °C. The Schopper-Riegler number (SR) is measured after 90 minutes (20 minutes pulping + 70 minutes maceration). The SR results are shown in the following tables:
pH 7.5 pH 9.5
The enzyme maceration results in a drainability improvement that varies with the pH and the type of pulp.

Claims

1. A pulping process wherein cellulase is used to improve the drainage properties of the pulp, characterized by a consistency above 8%.
2. A process according to Claim 1 wherein the raw material has an SR value above 25, and is preferably recycled fibre, waste paper or dried virgin pulp.
3. A process according to a preceding claim wherein the cellulase is derived from a strain of Asperqillus. Trichoderma. Humicola or Bacillus.
4. A process according to a preceding claim, wherein the pH is 4-6, and the cellulase is preferably derived from a strain of Aspergillus or Trichoderma.
5. A process according to any of Claims 1 - 3, wherein the pH is 6-
8.5, and the cellulase is preferably derived from a strain of Humicola or Bacillus.
6. A process for pulping and deinking of waste paper according to any of Claims 1 - 3, wherein the pulping is made at ph 6-9.5 in the presence of deinking chemicals, followed by separation of ink, and wherein the cellulase is preferably derived from Humicola or Bacillus.
7. A process according to a preceding claim, wherein the amount of cellulase corresponds to 250-5000 CEVU/kg of pulp dry matter.
EP91907253A 1990-03-29 1991-03-21 A pulping process using cellulase Revoked EP0524220B1 (en)

Applications Claiming Priority (3)

Application Number Priority Date Filing Date Title
DK080390A DK80390D0 (en) 1990-03-29 1990-03-29
DK803/90 1990-03-29
PCT/DK1991/000089 WO1991014822A1 (en) 1990-03-29 1991-03-21 A process using cellulase for improving drainage properties of pulp

Publications (2)

Publication Number Publication Date
EP0524220A1 true EP0524220A1 (en) 1993-01-27
EP0524220B1 EP0524220B1 (en) 1994-11-09

Family

ID=8097745

Family Applications (1)

Application Number Title Priority Date Filing Date
EP91907253A Revoked EP0524220B1 (en) 1990-03-29 1991-03-21 A pulping process using cellulase

Country Status (9)

Country Link
EP (1) EP0524220B1 (en)
JP (1) JP3014754B2 (en)
AT (1) ATE114004T1 (en)
CA (1) CA2079442C (en)
DE (1) DE69105124T2 (en)
DK (1) DK80390D0 (en)
ES (1) ES2065019T3 (en)
FI (1) FI924342A0 (en)
WO (1) WO1991014822A1 (en)

Cited By (1)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US8394237B2 (en) 2008-09-02 2013-03-12 BASF SE Ludwigshafen Method for manufacturing paper, cardboard and paperboard using endo-beta-1,4-glucanases as dewatering means

Families Citing this family (13)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
FR2701275B1 (en) * 1993-02-09 1995-03-17 Sibille Rech Method and installation for the recovery of cellulosic fibers of paper origin, and paper obtained from such recovered fibers.
EP0749473B1 (en) 1994-03-08 2005-10-12 Novozymes A/S Novel alkaline cellulases
CN102146362A (en) 1995-03-17 2011-08-10 诺沃奇梅兹有限公司 Noval endoglucanase
US6723549B2 (en) 1995-10-17 2004-04-20 Ab Enzymes Oy Cellulases, the genes encoding them and uses thereof
US6184019B1 (en) 1995-10-17 2001-02-06 Röhm Enzyme Finland OY Cellulases, the genes encoding them and uses thereof
AUPN909696A0 (en) * 1996-04-03 1996-04-26 Participant Project Ip Limited Paper pulp drainage aid
FI990444A (en) * 1998-03-11 1999-09-12 Nalco Chemical Co Increased pulp pulverization mode
KR100288119B1 (en) * 1998-06-27 2001-05-02 김충섭 Recycling Method of Corrugated Cardboard Using Flotation and Enzyme Treatment
KR20030035636A (en) * 2001-11-01 2003-05-09 한국화학연구원 Production method of saccharides from cellulose wastes in paper industry
US7922705B2 (en) 2005-10-03 2011-04-12 The Procter & Gamble Company Densified fibrous structures and methods for making same
BRPI0806921A2 (en) 2007-01-18 2014-04-29 Danisco Us Inc Genecor Division ENDOGLICANASE II MODIFIED AND METHODS OF USE
BRPI0816191B1 (en) 2007-09-03 2020-12-29 Novozymes A/S process for converting a material containing lignocellulose into a hydrolyzate
KR20130009762A (en) * 2010-02-12 2013-01-23 아크조 노벨 케미칼즈 인터내셔널 비.브이. Method for removing ink from paper

Family Cites Families (4)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
FR2604198B1 (en) * 1986-09-22 1989-07-07 Du Pin Cellulose PROCESS FOR TREATING A PAPER PULP WITH AN ENZYMATIC SOLUTION.
FR2629108A1 (en) * 1988-03-22 1989-09-29 Du Pin Cellulose PROCESS FOR PRODUCING PAPER OR CARTON FROM RECYCLED FIBERS TREATED WITH ENZYMES
FI81394C (en) * 1988-07-22 1993-07-20 Genencor Int Europ FOERFARANDE FOER BEHANDLING AV MASSA MED ENZYMER
KR960016598B1 (en) * 1989-05-16 1996-12-16 재단법인 한국화학연구소 Biological de-inking method

Non-Patent Citations (1)

* Cited by examiner, † Cited by third party
Title
See references of WO9114822A1 *

Cited By (1)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US8394237B2 (en) 2008-09-02 2013-03-12 BASF SE Ludwigshafen Method for manufacturing paper, cardboard and paperboard using endo-beta-1,4-glucanases as dewatering means

Also Published As

Publication number Publication date
CA2079442A1 (en) 1991-09-30
EP0524220B1 (en) 1994-11-09
JPH05505653A (en) 1993-08-19
DE69105124T2 (en) 1995-03-23
FI924342A (en) 1992-09-28
FI924342A0 (en) 1992-09-28
WO1991014822A1 (en) 1991-10-03
ATE114004T1 (en) 1994-11-15
DE69105124D1 (en) 1994-12-15
CA2079442C (en) 2002-09-10
JP3014754B2 (en) 2000-02-28
DK80390D0 (en) 1990-03-29
ES2065019T3 (en) 1995-02-01

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